Primary Events in Olfactory Reception
Abstract
This project was designed to characterize olfactory tissue-specific proteins previously identified with a library of monoclonal antibodies raised against frog olfactory cilia. First, we showed that our olfactory tissue- specific monoclonal antibodies all recognize different molecular forms of the same protein. We named this protein 'olfactomedin'. We then proceeded to purify olfactomedin and characterize it biochemically and immunohistochemically. We showed that olfactomedin is produced only in olfactory tissue by sustentacular cells and Bowman's glands and that it is deposited in the lower mucus layer of olfactory neuroepithelium. Next, we extracted mRNA from olfactory tissue and constructed a cDNA library. We obtained partial sequence information of the N- terminus of purified olfactomedin and used these data to design a degenerate oligonucleotide probe for the identification of a full-length cDNA clone which encodes olfactomedin. This clone was sequenced and found to encode a 448 amino acid protein preceded by a leader peptide of 16 amino acids. Analysis of the sequence showed no homologies with any known protein. Examination of its amino acid sequence by Chou-Fasman analysis in combination with biochemical and immunochemical evidence obtained previously enabled us to construct a model for olfactomedin which identifies this protein as a novel olfactory tissue-specific extracellular matrix protein, which forms the main structural component of the extracellular mucous matrix of olfactory neuropithelium and which may trigger the and differentiation of the dendritic knob and its olfactory cilia that house the olfactory transduction machinery.
Document Details
- Document Type
- Technical Report
- Publication Date
- Jan 08, 1993
- Accession Number
- ADA260562
Entities
People
- Robert R. Anholt
Organizations
- Duke University Hospital